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    Endophilin-A2 functions in membrane scission in clathrin-independent endocytosis

    Renard, H.-F. and Simunovic, M. and Lemière, J. and Boucrot, Emmanuel and Garcia-Castillo, M.D. and Arumugam, S. and Chambon, V. and Lamaze, C. and Wunder, C. and Kenworthy, A.K. and Schmidt, A.A. and McMahon, H.T. and Sykes, C. and Bassereau, P. and Johannes, L. (2015) Endophilin-A2 functions in membrane scission in clathrin-independent endocytosis. Nature 517 , pp. 493-496. ISSN 0028-0836.

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    Abstract

    During endocytosis, energy is invested to narrow the necks of cargo-containing plasma membrane invaginations to radii at which the opposing segments spontaneously coalesce, thereby leading to the detachment by scission of endocytic uptake carriers1. In the clathrin pathway, dynamin uses mechanical energy from GTP hydrolysis to this effect2, 3, 4, assisted by the BIN/amphiphysin/Rvs (BAR) domain-containing protein endophilin5, 6. Clathrin-independent endocytic events are often less reliant on dynamin7, and whether in these cases BAR domain proteins such as endophilin contribute to scission has remained unexplored. Here we show, in human and other mammalian cell lines, that endophilin-A2 (endoA2) specifically and functionally associates with very early uptake structures that are induced by the bacterial Shiga and cholera toxins, which are both clathrin-independent endocytic cargoes8. In controlled in vitro systems, endoA2 reshapes membranes before scission. Furthermore, we demonstrate that endoA2, dynamin and actin contribute in parallel to the scission of Shiga-toxin-induced tubules. Our results establish a novel function of endoA2 in clathrin-independent endocytosis. They document that distinct scission factors operate in an additive manner, and predict that specificity within a given uptake process arises from defined combinations of universal modules. Our findings highlight a previously unnoticed link between membrane scaffolding by endoA2 and pulling-force-driven dynamic scission.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 18 Dec 2014 12:09
    Last Modified: 06 Dec 2016 11:15
    URI: http://eprints.bbk.ac.uk/id/eprint/11323

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